Carboxypeptidase M

Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.

Carboxypeptidase M Related Areas

Enzyme>>Protease & Regulator>>Carboxypeptidase & Regulator>>Carboxypeptidase M/CPM

Carboxypeptidase M Alternative Names

Carboxypeptidase M, CPM [Homo sapiens]

Carboxypeptidase M, Cpm, 1110060I01Rik, 5730456K23Rik, AA589379, E030045M14Rik, MGC118152 [Mus musculus]

Summaries for Carboxypeptidase M

Entrez Gene summary for Carboxypeptidase M:

The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.

OMIM - description for Carboxypeptidase M:

Carboxypeptidases specifically remove COOH-terminal basic amino acids (arginine or lysine). They have important functions in many biologic processes, including activation, inactivation, or modulation of peptide hormone activity and alteration of physical properties of proteins and enzymes. Carboxypeptidase M is a membrane-bound arginine/lysine carboxypeptidase found in many tissues and cultured cells. Rehli et al. (1995) found that its expression associated with monocyte to macrophage differentiation. Tan et al. (1989) described the molecular cloning and sequencing of the cDNA for human carboxypeptidase M from a human placental cDNA library. The 2-kb cDNA contained an open reading frame of 1,317 basepairs, encoding a 439-amino acid protein. Sequence analysis revealed hydrophobic regions at the NH(2) and carboxy termini. There are 6 potential asparagine-linked glycosylation sites. Observed sequence homologies with other carboxypeptidases were as follows: human plasma carboxypeptidase N (212070), 41%; bovine carboxypeptidase H (114855), 41%; and bovine pancreatic carboxypeptidases A and B, 15%. The active site residues of carboxypeptidases A and B are conserved in carboxypeptidase M.

Wikipedia summary for Carboxypeptidase M:

Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene.[1][2] The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.

Human Carboxypeptidase M Protein General Information

 

• Protein names: Recommended name: Carboxypeptidase M Short name=CPM
• Sequence length: 443 AA.
• Domain: Signal
• Sequence similarities: Belongs to the peptidase M14 family.
• Catalytic activity: Cleavage of C-terminal arginine or lysine residues from polypeptides.
• Cofactor: Binds 1 zinc ion per subunit.
• Subcellular location: Cell membrane; Lipid-anchor › GPI-anchor
• Enzyme regulation: Inhibited by O-phenanthroline and MGTA and activated by cobalt.

General information above from UniProt

Function for Carboxypeptidase M Protein

UniProtKB:

Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.

Genatlas:

• carboxypeptidase M cleaving basic C terminal amino acids in monocyte to macrophage differentiation